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PDBsum entry 1z1y
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Cell adhesion
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PDB id
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1z1y
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References listed in PDB file
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Key reference
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Title
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The essential mosquito-Stage p25 and p28 proteins from plasmodium form tile-Like triangular prisms.
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Authors
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A.K.Saxena,
K.Singh,
H.P.Su,
M.M.Klein,
A.W.Stowers,
A.J.Saul,
C.A.Long,
D.N.Garboczi.
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Ref.
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Nat Struct Mol Biol, 2006,
13,
90-91.
[DOI no: ]
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PubMed id
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Abstract
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P25 and P28 proteins are essential for Plasmodium parasites to infect mosquitoes
and are leading candidates for a transmission-blocking malaria vaccine. The
Plasmodium vivax P25 is a triangular prism that could tile the parasite surface.
The residues forming the triangle are conserved in P25 and P28 from all
Plasmodium species. A cocrystal structure shows that a transmission-blocking
antibody uses only its heavy chain to bind Pvs25 at a vertex of the triangle.
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Figure 1.
Figure 1. Views of Pvs25. (a) The triangular prism formed by
domain 1 (light blue), domain 2 (green), domain 3 (red) and
domain 4 (gold). The central -strands
in each domain are labeled 1 and 2. The 11 disulfide bonds
(violet) are shown. (b) View of the edge of the prism. (c) Pvs25
forms sheets in the crystals. One molecule (red) makes contacts
with four 2[1] symmetry mates (light blue) and two molecules
related by lattice translations (dark blue). The six light blue
molecules all have the same triangular face 'up', whereas the
other three molecules (red and dark blue) all have the opposite
face 'up'. As P25 and P28 molecules are thin prisms, the
glycosylphosphatidylinositol anchor could reach the cell
membrane whether a molecule was facing 'up' or 'down' on the
membrane. N term, N terminus; C term, C terminus.
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Figure 2.
Figure 2. Binding of transmission-blocking antibodies to Pvs25.
(a) 2A8 Fab bound via its heavy chain (dark blue) to the B
loop of Pvs25 domain 2. The light chain (light blue) does not
contact Pvs25. The B loop of Pvs25 domain 3 (red) extends up
from the plane of the triangle. (b) Monoclonal antibodies 1H10
and 1A5 do not bind in the presence of prebound 2A8. With Pvs25
immobilized on a Biacore chip, 2A8 was injected at (i) until
binding was saturated at (ii), and then the second antibody and
2A8 were injected at (iii) until (iv). Buffer without protein
was injected from (ii) to (iii) and from (iv) onward.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2006,
13,
90-91)
copyright 2006.
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